OBGC_ARATH
ID OBGC_ARATH Reviewed; 681 AA.
AC Q8L7L0;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTP-binding protein OBGC, chloroplastic;
DE Short=AtOBGC;
DE AltName: Full=GTP-binding protein OBG-like;
DE Short=AtOBGL;
DE AltName: Full=Protein CHLOROPLASTIC SAR1;
DE Short=CPSAR1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 269;
DE AltName: Full=Protein EMBRYO DEFECTIVE 3138;
DE Flags: Precursor;
GN Name=OBGL; Synonyms=EMB269, EMB3138; OrderedLocusNames=At5g18570;
GN ORFNames=T28N17.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19995735; DOI=10.1093/mp/ssp073;
RA Chigri F., Sippel C., Kolb M., Vothknecht U.C.;
RT "Arabidopsis OBG-like GTPase (AtOBGL) is localized in chloroplasts and has
RT an essential function in embryo development.";
RL Mol. Plant 2:1373-1383(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19636801; DOI=10.1007/s11103-009-9529-3;
RA Bang W.Y., Hata A., Jeong I.S., Umeda T., Masuda T., Chen J., Yoko I.,
RA Suwayxstika I.N., Kim D.W., Im C.H., Lee B.H., Lee Y., Lee K.W., Shiina T.,
RA Bahk J.D.;
RT "AtObgC, a plant ortholog of bacterial Obg, is a chloroplast-targeting
RT GTPase essential for early embryogenesis.";
RL Plant Mol. Biol. 71:379-390(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20408996; DOI=10.1111/j.1365-313x.2010.04225.x;
RA Garcia C., Khan N.Z., Nannmark U., Aronsson H.;
RT "The chloroplast protein CPSAR1, dually localized in the stroma and the
RT inner envelope membrane, is involved in thylakoid biogenesis.";
RL Plant J. 63:73-85(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22380942; DOI=10.1111/j.1365-313x.2012.04976.x;
RA Bang W.Y., Chen J., Jeong I.S., Kim S.W., Kim C.W., Jung H.S., Lee K.H.,
RA Kweon H.S., Yoko I., Shiina T., Bahk J.D.;
RT "Functional characterization of ObgC in ribosome biogenesis during
RT chloroplast development.";
RL Plant J. 71:122-134(2012).
CC -!- FUNCTION: GTP-binding protein involved in membrane biogenesis and
CC protein synthesis in chloroplast. Functions in the biogenesis of
CC thylakoid membrane and plastid ribosome during chloroplast development.
CC May be involved in the vesicular traffic between the chloroplast inner
CC envelope membrane and thylakoids. Possesses GTPase activity in vitro.
CC {ECO:0000269|PubMed:19636801, ECO:0000269|PubMed:19995735,
CC ECO:0000269|PubMed:20408996, ECO:0000269|PubMed:22380942}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast
CC inner membrane. Note=Exhibits a punctate staining pattern.
CC -!- TISSUE SPECIFICITY: Specifically expressed in leaves.
CC {ECO:0000269|PubMed:19636801}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous. Embryo
CC maturation arrested at the late globular stage.
CC {ECO:0000269|PubMed:19636801, ECO:0000269|PubMed:19995735,
CC ECO:0000269|PubMed:20408996, ECO:0000269|PubMed:22380942}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000305}.
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DR EMBL; AC069328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92580.1; -; Genomic_DNA.
DR EMBL; AY128395; AAM91598.1; -; mRNA.
DR EMBL; BT008421; AAP37780.1; -; mRNA.
DR RefSeq; NP_197358.2; NM_121862.3.
DR AlphaFoldDB; Q8L7L0; -.
DR SMR; Q8L7L0; -.
DR BioGRID; 17251; 1.
DR STRING; 3702.AT5G18570.1; -.
DR iPTMnet; Q8L7L0; -.
DR PaxDb; Q8L7L0; -.
DR PRIDE; Q8L7L0; -.
DR ProteomicsDB; 250954; -.
DR EnsemblPlants; AT5G18570.1; AT5G18570.1; AT5G18570.
DR GeneID; 831975; -.
DR Gramene; AT5G18570.1; AT5G18570.1; AT5G18570.
DR KEGG; ath:AT5G18570; -.
DR Araport; AT5G18570; -.
DR TAIR; locus:2182998; AT5G18570.
DR eggNOG; KOG1489; Eukaryota.
DR HOGENOM; CLU_011747_4_0_1; -.
DR InParanoid; Q8L7L0; -.
DR OMA; TDSIKWP; -.
DR OrthoDB; 1150635at2759; -.
DR PhylomeDB; Q8L7L0; -.
DR PRO; PR:Q8L7L0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7L0; baseline and differential.
DR Genevisible; Q8L7L0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.30.300.350; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01454; GTPase_Obg; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR InterPro; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR015349; OCT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF09269; DUF1967; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF102741; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
DR PROSITE; PS51881; OCT; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; GTP-binding; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Plastid inner membrane; Reference proteome;
KW Ribosome biogenesis; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..681
FT /note="GTP-binding protein OBGC, chloroplastic"
FT /id="PRO_0000424827"
FT DOMAIN 208..378
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 379..547
FT /note="OBG-type G"
FT DOMAIN 577..656
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 25..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 385..392
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 410..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 432..435
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 499..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 528..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 681 AA; 75648 MW; FC61BB8BA5EA9EDB CRC64;
MASISINCFF TPQALARPSR TRKIFAKPDK VSGRTRSPRK TKLQREVELK SRGGDKLQPV
SDAGGEATTY TRLPPREDYY DVSLLSSSYL KVSEEVKLSE SNVARVEEKI ETLREIEEEE
KEKEVKSYDD DDIWGNYRRL DVFEGSSRSI DEDDEDWEDE VFEYGDETDA EKDDSEGSEL
KDGEVLCFSG EEEEDEIGVK EKGVPAVMRC FDRAKIYVRA GDGGNGVVAF RREKFVPFGG
PSGGDGGRGG NVYVEVDGSM NSLLPFRKSV HFRAGRGEHG RGKMQSGAKG DNVVVKVAPG
TVVRQAREVG SEVEGEEGEE KEVLLELLHP GQRALLLPGG RGGRGNASFK SGMNKVPRIA
ENGEEGPEMW LDLELKLVAD VGIVGAPNAG KSTLLSVISA AQPTIANYPF TTLLPNLGVV
SFDYDSTMVV ADLPGLLEGA HRGFGLGHEF LRHTERCSAL VHVVDGSAPQ PELEFEAVRL
ELELFSPEIA EKPYVVAYNK MDLPDAYEKW PMFQETLRAR GIEPFCMSAV QREGTHEVIS
SVYELLKKYR AANAEPKALF DQANENLDHV AKKIDKERRA AINEFEVFRD SGTRAWHVVG
AGLQRFVQMT NWRYMDSDKR FQHVLDACGV NKSLKNMGVK EGDTVIVGEM ELIWHDSANG
SSRPTDSNKT STDSVRWPQW K
